On August 17, the Tsinghua News Network reported that tendinopathy, a common musculoskeletal condition, frequently results in persistent pain, reduced athletic prowess, and a heightened likelihood of spontaneous tendon rupture. Among the various factors contributing to this condition, transforming growth factor beta 1 (TGF-β1) emerges as a primary instigator of tendon fibrosis and irregular collagen deposition. The crux of treating tendinopathy lies in the precise capture of excessive TGF-β1 at the site of the affected tendon, while maintaining its normal physiological roles. Recently, a pioneering strategy has been introduced by a team helmed by Yu Jiakuo, the director of the Orthopedics and Sports Medicine Center at Beijing Tsinghua Changgung Hospital, Tsinghua University. This novel method employs a fully natural self-assembling peptide to trap TGF-β1 in situ at the tendon injury site, thereby reshaping the tendon's pathological microenvironment.

The team engineered a modular self-assembling peptide, AsPep-FTSQ, crafted entirely from natural amino acids. Upon local injection, it autonomously forms a nanofiber network within the tendon lesion, persistently capturing surplus free TGF-β1 in the vicinity. This action effectively curtails aberrant profibrotic signaling, restrains the pathological transformation of tendon cells, and fosters the reorientation of collagen fibers in alignment with the tendon's primary stress direction. The efficacy of this approach in structural repair and functional enhancement has been substantiated through studies conducted on rat and beagle models of tendinopathy.